Validity of putative calcium binding loops of photoprotein aequorin

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Site-specific mutagenesis of the calcium-binding photoprotein aequorin.

The luminescent protein aequorin from the jellyfish Aequoria victoria emits light by an intramolecular reaction in the presence of a trace amount of Ca(2+). In order to understand the mechanism of the reaction, a study of structure-function relationships was undertaken with respect to modifying certain of its amino acid residues. This was done by carrying out oligonucleotide-directed site-speci...

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Measurement of ionized calcium in blood platelets with the photoprotein aequorin. Comparison with Quin 2.

The Ca2+-sensitive photoprotein aequorin (Mr = 20,000) was introduced into human blood platelets by incubation with 10 mM EGTA and 5 mM ATP. Platelet cytoplasmic and granule contents were retained during the loading procedure, and platelet morphology, aggregation, and secretion in response to agonists were normal after aequorin loading. Luminescence indicated an apparent resting cytoplasmic ion...

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Bioluminescence of the Ca(2+)-binding photoprotein, aequorin, after histidine modification.

Modification studies of the 5 histidine residues in aequorin employing site-directed mutagenesis and diethyl pyrocarbonate suggested that His169 may be the site of binding of molecular oxygen in aequorin. The modification of this residue led to complete loss of activity, whereas modification of the remaining 4 histidine residues yielded mutant aequorins with varying bioluminescence activities.

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Peroxidized coelenterazine, the active group in the photoprotein aequorin.

The photoprotein aequorin emits light by an intramolecular reaction when Ca2+ is added under either aerobic or anaerobic conditions. Previously reported evidence has indicated two possibilities: (i) the functional group of aequorin is coelenterazine itself, a compond that plays key roles in the bioluminescence of various other types of organisms, or (ii) it is the enolized form of this compound...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 1992

ISSN: 0014-5793

DOI: 10.1016/0014-5793(92)80693-b